(data stored in SCRATCH zone)

SWISSPROT: A0A0H2ZJY3_PSEAB

ID   A0A0H2ZJY3_PSEAB        Unreviewed;       434 AA.
AC   A0A0H2ZJY3;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 13.
DE   SubName: Full=Putative tRNA and rRNA cytosine-C5-methylases {ECO:0000313|EMBL:ABJ14973.1};
GN   Name=sun {ECO:0000313|EMBL:ABJ14973.1};
GN   OrderedLocusNames=PA14_00180 {ECO:0000313|EMBL:ABJ14973.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ14973.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ14973.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ14973.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- FUNCTION: Specifically methylates the cytosine at position 967
CC       (m5C967) of 16S rRNA. {ECO:0000256|SAAS:SAAS00672432}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + cytosine(967) in 16S
CC       rRNA = S-adenosyl-L-homocysteine + 5-methylcytosine(967) in 16S
CC       rRNA. {ECO:0000256|SAAS:SAAS00672435}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00633808}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. RsmB/NOP family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01023,
CC       ECO:0000256|SAAS:SAAS00637407}.
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DR   EMBL; CP000438; ABJ14973.1; -; Genomic_DNA.
DR   RefSeq; WP_003142203.1; NC_008463.1.
DR   ProteinModelPortal; A0A0H2ZJY3; -.
DR   EnsemblBacteria; ABJ14973; ABJ14973; PA14_00180.
DR   KEGG; pau:PA14_00180; -.
DR   KO; K03500; -.
DR   OMA; LRVNRQH; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008649; F:rRNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.940.10; -; 1.
DR   InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR   InterPro; IPR001678; MeTrfase_RsmB/NOP2.
DR   InterPro; IPR006027; NusB_RsmB_TIM44.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR004573; rRNA_ssu_MeTfrase_B.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   Pfam; PF01029; NusB; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF48013; SSF48013; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00563; rsmB; 1.
DR   PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0H2ZJY3.
DR   SWISS-2DPAGE; A0A0H2ZJY3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00633812};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00637415, ECO:0000313|EMBL:ABJ14973.1};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00637422};
KW   rRNA processing {ECO:0000256|SAAS:SAAS00633795};
KW   S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00637399};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU01023,
KW   ECO:0000256|SAAS:SAAS00637429}.
FT   DOMAIN      161    431       SAM_MT_RSMB_NOP. {ECO:0000259|PROSITE:
FT                                PS51686}.
FT   ACT_SITE    373    373       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01023}.
FT   BINDING     275    275       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     301    301       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
FT   BINDING     320    320       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PROSITE-ProRule:PRU01023}.
SQ   SEQUENCE   434 AA;  47128 MW;  F1AA7AB054F6300B CRC64;
     MNPRLAACQA LAAVLAGRAS LSGALPPQLD KVAPRDRGLT QELAFGAARW QPRLQALAAR
     LLQKPFKAAD TDIHALLLIG LYQLLYTRIP PHAAIGETVG CADKLKKGWA KGVLNAVLRR
     AQREGETLLA EVDRDPSARL GHPRWLLKAL KQAWPEQLDT LCAANNAHPP MTLRVNRRHG
     ERDAYLAELA EAGIEARACD YSRDGIQLAA PRDVRELPGF AEGRVSVQDE ATQLAAELLE
     SAPGQRVLDA CCAPGGKTCH LLETQPGLAE VVAVDLEESR LVRVRENLQR LGLQASLVAA
     DARATGEWWD GKPFQRILLD APCSATGVIR RHPDIKLARK PEDIAALAHL QGELLDALWP
     TLEVGGVLLY ATCSVMPAEN SDSIAAFLAR TPGARELDLP GPWGMKQPHG RQLLPQVEGH
     DGFYYAKLIK ISAR
//

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